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Protein

Phenylalanine-4-hydroxylase

Gene

phhA

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin.

Cofactori

Pathwayi: L-phenylalanine degradation

This protein is involved in step 1 of the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Phenylalanine-4-hydroxylase (phhA)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. no protein annotated in this organism
This subpathway is part of the pathway L-phenylalanine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine, the pathway L-phenylalanine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi138 – 1381Iron
Metal bindingi143 – 1431Iron
Metal bindingi184 – 1841Iron

GO - Molecular functioni

  • iron ion binding Source: InterPro
  • phenylalanine 4-monooxygenase activity Source: CACAO

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Phenylalanine catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciCVIO243365:GHUD-3249-MONOMER.
MetaCyc:MONOMER-12067.
BRENDAi1.14.16.1. 1370.
UniPathwayiUPA00139; UER00337.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine-4-hydroxylase (EC:1.14.16.1)
Short name:
PAH
Alternative name(s):
Phe-4-monooxygenase
Gene namesi
Name:phhA
Ordered Locus Names:CV_3180
OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Taxonomic identifieri243365 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
Proteomesi
  • UP000001424 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297Phenylalanine-4-hydroxylasePRO_0000205553Add
BLAST

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi243365.CV_3180.

Structurei

Secondary structure

1
297
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 165Combined sources
Turni17 – 193Combined sources
Turni24 – 263Combined sources
Helixi33 – 353Combined sources
Helixi38 – 5417Combined sources
Turni56 – 583Combined sources
Helixi61 – 699Combined sources
Beta strandi74 – 763Combined sources
Helixi80 – 9112Combined sources
Beta strandi94 – 1018Combined sources
Helixi104 – 1129Combined sources
Beta strandi115 – 1195Combined sources
Helixi125 – 1273Combined sources
Beta strandi128 – 1303Combined sources
Helixi136 – 1438Combined sources
Helixi145 – 1484Combined sources
Helixi150 – 16112Combined sources
Helixi163 – 1686Combined sources
Helixi172 – 18110Combined sources
Turni182 – 1854Combined sources
Beta strandi187 – 1904Combined sources
Beta strandi193 – 1964Combined sources
Helixi199 – 2024Combined sources
Helixi207 – 2137Combined sources
Beta strandi215 – 2217Combined sources
Helixi224 – 2285Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi239 – 2457Combined sources
Helixi247 – 2537Combined sources
Helixi259 – 2668Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LTUX-ray1.74A1-297[»]
1LTVX-ray2.00A1-297[»]
1LTZX-ray1.40A1-297[»]
3TCYX-ray1.55A1-297[»]
3TK2X-ray1.35A1-297[»]
3TK4X-ray1.50A1-297[»]
4ESMX-ray1.35A1-297[»]
4ETLX-ray1.49A1-297[»]
4JPXX-ray1.55A1-297[»]
4JPYX-ray2.13A1-297[»]
4Q3WX-ray1.40A1-297[»]
4Q3XX-ray1.35A1-297[»]
4Q3YX-ray1.40A1-297[»]
4Q3ZX-ray1.35A1-297[»]
ProteinModelPortaliP30967.
SMRiP30967. Positions 2-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30967.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105MIR. Bacteria.
COG3186. LUCA.
HOGENOMiHOG000253806.
KOiK00500.
OMAiHEVFGHC.
OrthoDBiEOG6W7200.

Family and domain databases

Gene3Di1.10.800.10. 1 hit.
InterProiIPR001273. ArAA_hydroxylase.
IPR018301. ArAA_hydroxylase_Fe/CU_BS.
IPR019774. Aromatic-AA_hydroxylase_C.
IPR005960. Phe-4-hydroxylase_mono.
[Graphical view]
PANTHERiPTHR11473. PTHR11473. 1 hit.
PfamiPF00351. Biopterin_H. 1 hit.
[Graphical view]
PRINTSiPR00372. FYWHYDRXLASE.
SUPFAMiSSF56534. SSF56534. 1 hit.
TIGRFAMsiTIGR01267. Phe4hydrox_mono. 1 hit.
PROSITEiPS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30967-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDRADFVVP DITTRKNVGL SHDANDFTLP QPLDRYSAED HATWATLYQR
60 70 80 90 100
QCKLLPGRAC DEFMEGLERL EVDADRVPDF NKLNQKLMAA TGWKIVAVPG
110 120 130 140 150
LIPDDVFFEH LANRRFPVTW WLREPHQLDY LQEPDVFHDL FGHVPLLINP
160 170 180 190 200
VFADYLEAYG KGGVKAKALG ALPMLARLYW YTVEFGLINT PAGMRIYGAG
210 220 230 240 250
ILSSKSESIY CLDSASPNRV GFDLMRIMNT RYRIDTFQKT YFVIDSFKQL
260 270 280 290
FDATAPDFAP LYLQLADAQP WGAGDVAPDD LVLNAGDRQG WADTEDV
Length:297
Mass (Da):33,616
Last modified:October 24, 2003 - v4
Checksum:i6D29A04203E906FD
GO

Sequence cautioni

The sequence AAA23115.1 differs from that shown. Reason: Frameshift at position 172. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641M → L (PubMed:1655752).Curated
Sequence conflicti64 – 641M → L (Ref. 2) Curated
Sequence conflicti85 – 851Q → E (PubMed:1655752).Curated
Sequence conflicti85 – 851Q → E (Ref. 2) Curated
Sequence conflicti276 – 2761V → I (PubMed:1655752).Curated
Sequence conflicti276 – 2761V → I (Ref. 2) Curated
Sequence conflicti288 – 2881R → H (PubMed:1655752).Curated
Sequence conflicti288 – 2881R → H (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55915 Genomic DNA. Translation: AAA23115.1. Frameshift.
AF146711 Genomic DNA. Translation: AAD37774.1.
AE016825 Genomic DNA. Translation: AAQ60846.1.
PIRiA40996.

Genome annotation databases

EnsemblBacteriaiAAQ60846; AAQ60846; CV_3180.
KEGGicvi:CV_3180.
PATRICi21441114. VBIChrVio67196_3099.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55915 Genomic DNA. Translation: AAA23115.1. Frameshift.
AF146711 Genomic DNA. Translation: AAD37774.1.
AE016825 Genomic DNA. Translation: AAQ60846.1.
PIRiA40996.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LTUX-ray1.74A1-297[»]
1LTVX-ray2.00A1-297[»]
1LTZX-ray1.40A1-297[»]
3TCYX-ray1.55A1-297[»]
3TK2X-ray1.35A1-297[»]
3TK4X-ray1.50A1-297[»]
4ESMX-ray1.35A1-297[»]
4ETLX-ray1.49A1-297[»]
4JPXX-ray1.55A1-297[»]
4JPYX-ray2.13A1-297[»]
4Q3WX-ray1.40A1-297[»]
4Q3XX-ray1.35A1-297[»]
4Q3YX-ray1.40A1-297[»]
4Q3ZX-ray1.35A1-297[»]
ProteinModelPortaliP30967.
SMRiP30967. Positions 2-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243365.CV_3180.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ60846; AAQ60846; CV_3180.
KEGGicvi:CV_3180.
PATRICi21441114. VBIChrVio67196_3099.

Phylogenomic databases

eggNOGiENOG4105MIR. Bacteria.
COG3186. LUCA.
HOGENOMiHOG000253806.
KOiK00500.
OMAiHEVFGHC.
OrthoDBiEOG6W7200.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00337.
BioCyciCVIO243365:GHUD-3249-MONOMER.
MetaCyc:MONOMER-12067.
BRENDAi1.14.16.1. 1370.

Miscellaneous databases

EvolutionaryTraceiP30967.

Family and domain databases

Gene3Di1.10.800.10. 1 hit.
InterProiIPR001273. ArAA_hydroxylase.
IPR018301. ArAA_hydroxylase_Fe/CU_BS.
IPR019774. Aromatic-AA_hydroxylase_C.
IPR005960. Phe-4-hydroxylase_mono.
[Graphical view]
PANTHERiPTHR11473. PTHR11473. 1 hit.
PfamiPF00351. Biopterin_H. 1 hit.
[Graphical view]
PRINTSiPR00372. FYWHYDRXLASE.
SUPFAMiSSF56534. SSF56534. 1 hit.
TIGRFAMsiTIGR01267. Phe4hydrox_mono. 1 hit.
PROSITEiPS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of Chromobacterium violaceum phenylalanine hydroxylase in Escherichia coli and comparison of amino acid sequence with mammalian aromatic amino acid hydroxylases."
    Onishi A., Liotta L.J., Benkovic S.J.
    J. Biol. Chem. 266:18454-18459(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20.
    Strain: ATCC 12540 / LMG 3962 / NCTC 9695.
  2. "Expression, isolation, and metal-dependent catalysis of phenylalanine hydroxylase from Chromobacterium violaceum."
    Volner A., Nersissian A.M., Abu-Omar M.M.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 12540 / LMG 3962 / NCTC 9695.
  3. "The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
    Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A.
    , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
    Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.
  4. "Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates."
    Erlandsen H., Kim J.Y., Patch M.G., Han A., Volner A., Abu-Omar M.M., Stevens R.C.
    J. Mol. Biol. 320:645-661(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).

Entry informationi

Entry nameiPH4H_CHRVO
AccessioniPrimary (citable) accession number: P30967
Secondary accession number(s): Q9R634, Q9XC88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 24, 2003
Last modified: November 11, 2015
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.